Phosphorylation and inactivation of HMG‐CoA reductase at the AMP‐activated protein kinase site in response to fructose treatment of isolated rat hepatocytes

FEBS Letters

Hardie, D.Grahame¹  Gillespie, John G.¹ 

[1] Department of Biochemistry, The University, Dundee DD1 4HN, Scotland, UK

关键词: HMG-CoA reductase;    Cholesterol synthesis;    Protein kinase;    Phosphorylation site;    Protein phosphorylation;    Hepatocyte;   

DOI  :  10.1016/0014-5793(92)80837-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have previously shown that incubation of isolated hepatocytes with fructose leads to elevation of AMP and activation of the AMP-activated protein kinase. We now show that this treatment causes marked inactivation of HMG-CoA reductase. Using immunoprecipitation from the microsomal fraction of ³²P-labelled cells, we also show that this treatment leads to a 2.6-fold increase in the phosphorylation of the 100 kDa subunit of HMG-CoA reductase. Successive digestion of this ³²P-labelled subunit with cyanogen bromide and endoproteinase Lys-C confirmed that Ser-871 the site phosphorylated in cell-free assays by the AMP-activated protein kinase, was the only site phosphorylated under these conditions.

【 授权许可】

Unknown